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Canine Immunoglobulin E (IgE) is a specialized antibody isotype that plays a central role in the canine immune system, particularly in mediating type I hypersensitivity reactions and providing defense against parasitic infections, such as helminths (3, 13). Structurally, it consists of two heavy epsilon chains and two light chains, characterized by its ability to bind with high affinity to the FcεRI receptor on mast cells and basophils (13). Upon cross-linking by allergens, IgE triggers the degranulation of these cells, releasing inflammatory mediators like histamine and cytokines that drive the clinical signs of allergy, most notably in canine atopic dermatitis (CAD) and flea allergy dermatitis (1, 8). Interestingly, dogs exhibit significantly higher basal serum IgE levels compared to humans—often up to 100 times higher—which is frequently attributed to a higher prevalence of parasitic exposure and presents a unique challenge for therapeutic neutralization (6, 7). While current approved treatments for canine allergies, such as lokivetmab, target downstream cytokines like IL-31, canine IgE remains a major therapeutic target for the development of anti-IgE monoclonal antibodies and vaccines aimed at reducing free IgE levels and downregulating its receptors (2, 18). Experimental studies have demonstrated that neutralizing canine IgE can effectively reduce IgE-bearing cells and plasma IgE concentrations, mirroring the clinical success of omalizumab in human medicine (2, 9).
Neutralization of free IgE and prevention of binding to high-affinity IgE receptors (FcεRI) on mast cells and basophils, leading to reduced inflammatory mediator release.
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